PMID: 8950374Nov 12, 1996Paper

Biochemical and spectroscopic properties of the four-subunit quinol oxidase (cytochrome ba3) from Paracoccus denitrificans

Biochimica Et Biophysica Acta
I ZickermannB Ludwig

Abstract

The ba3 quinol oxidase from Paracoccus denitrificans has been purified by a new protocol leading to significantly higher yields than previously reported (Richter et al. (1994) J. Biol. Chem. 269, 23079-23086). In an SDS PAG an additional protein band compared with the previous preparation appears, which can be identified as the major form of subunit II. All protein bands can be assigned to genes of the qox operon by N-terminal sequencing, indicating that the oxidase consists of four subunits. In addition to one heme A, one heme B, and one copper atom, the preparation contains two ubiquinone molecules per enzyme. The oxidase is further characterized by electron paramagnetic resonance (EPR), circular dichroism (CD) and magnetic circular dichroism (MCD) spectroscopy.

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Citations

Nov 27, 2007·Hypertension Research : Official Journal of the Japanese Society of Hypertension·Tomoko ShinzatoShuichi Takishita
Dec 25, 2008·Journal of Oral Science·Motohiko YagiKoichi Ito
Jun 27, 2009·Journal of Atherosclerosis and Thrombosis·Takeshi AraiAkiyo Matsumoto
Jun 28, 2008·Biochimica Et Biophysica Acta·Freya A BundschuhBernd Ludwig
Jul 3, 1998·FEBS Letters·M S MuntyanN P Starshinova
Mar 28, 1997·The Journal of Biological Chemistry·M GleissnerG Schäfer
May 28, 2013·Nature Materials·Sergey Borisenko
Jan 12, 1999·Journal of Bacteriology·J BengtssonL Hederstedt
Dec 5, 1998·Microbiology and Molecular Biology Reviews : MMBR·S C BakerR J van Spanning

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